TATCD_BACSU
ID TATCD_BACSU Reviewed; 242 AA.
AC P42252; O31468;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 4.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Sec-independent protein translocase protein TatCd {ECO:0000255|HAMAP-Rule:MF_00902};
GN Name=tatC1 {ECO:0000255|HAMAP-Rule:MF_00902}; Synonyms=tatCd, ycbT;
GN OrderedLocusNames=BSU02640;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7704254; DOI=10.1099/13500872-141-2-269;
RA Ogawa K., Akagawa E., Nakamura K., Yamane K.;
RT "Determination of a 21548 bp nucleotide sequence around the 24 degrees
RT region of the Bacillus subtilis chromosome.";
RL Microbiology 141:269-275(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 101 AND 104.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 187-242.
RC STRAIN=168;
RX PubMed=1353026; DOI=10.1016/0014-5793(92)80656-2;
RA Awade A., Cleuziat P., Gonzales T., Robert-Baudouy J.;
RT "Characterization of the pcp gene encoding the pyrrolidone carboxyl
RT peptidase of Bacillus subtilis.";
RL FEBS Lett. 305:67-73(1992).
RN [5]
RP IDENTIFICATION OF THE TAT GENES, AND SECRETION OF PHOD.
RX PubMed=11007775; DOI=10.1074/jbc.m004887200;
RA Jongbloed J.D.H., Martin U., Antelmann H., Hecker M., Tjalsma H.,
RA Venema G., Bron S., van Dijl J.M., Mueller J.;
RT "TatC is a specificity determinant for protein secretion via the twin-
RT arginine translocation pathway.";
RL J. Biol. Chem. 275:41350-41357(2000).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=12867413; DOI=10.1074/jbc.m306516200;
RA Pop O.I., Westermann M., Volkmer-Engert R., Schulz D., Lemke C.,
RA Schreiber S., Gerlach R., Wetzker R., Mueller J.P.;
RT "Sequence-specific binding of prePhoD to soluble TatAd indicates protein-
RT mediated targeting of the Tat export in Bacillus subtilis.";
RL J. Biol. Chem. 278:38428-38436(2003).
RN [7]
RP CHARACTERIZATION OF THE TWO TAT TRANSLOCASE SYSTEMS.
RX PubMed=15554971; DOI=10.1111/j.1365-2958.2004.04341.x;
RA Jongbloed J.D.H., Grieger U., Antelmann H., Hecker M., Nijland R., Bron S.,
RA van Dijl J.M.;
RT "Two minimal Tat translocases in Bacillus.";
RL Mol. Microbiol. 54:1319-1325(2004).
RN [8]
RP INTERACTION WITH TATAD, AND DISRUPTION PHENOTYPE.
RX PubMed=16698798; DOI=10.1074/jbc.m513900200;
RA Schreiber S., Stengel R., Westermann M., Volkmer-Engert R., Pop O.I.,
RA Mueller J.P.;
RT "Affinity of TatCd for TatAd elucidates its receptor function in the
RT Bacillus subtilis twin arginine translocation (Tat) translocase system.";
RL J. Biol. Chem. 281:19977-19984(2006).
RN [9]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=168;
RX PubMed=18029357; DOI=10.1074/jbc.m708134200;
RA Barnett J.P., Eijlander R.T., Kuipers O.P., Robinson C.;
RT "A minimal Tat system from a gram-positive organism: a bifunctional TatA
RT subunit participates in discrete TatAC and TatA complexes.";
RL J. Biol. Chem. 283:2534-2542(2008).
CC -!- FUNCTION: Part of the twin-arginine translocation (Tat) system that
CC transports large folded proteins containing a characteristic twin-
CC arginine motif in their signal peptide across membranes. Required for
CC PhoD secretion. TatCd promotes membrane localization of TatAd via
CC domain specific interactions. TatCd is required for stabile production
CC of TatAd as well as for its maintenance. {ECO:0000255|HAMAP-
CC Rule:MF_00902, ECO:0000269|PubMed:18029357}.
CC -!- SUBUNIT: Forms a complex with TatAd. Two types of complexes exist: one
CC composed of TatAd and TatCd, and another composed only of TatAd.
CC {ECO:0000255|HAMAP-Rule:MF_00902, ECO:0000269|PubMed:18029357}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00902,
CC ECO:0000269|PubMed:12867413}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00902, ECO:0000269|PubMed:12867413}.
CC -!- INDUCTION: Expressed under conditions of phosphate starvation.
CC -!- DISRUPTION PHENOTYPE: Depletion of TatCd results in a drastic reduction
CC of TatAd. {ECO:0000269|PubMed:16698798}.
CC -!- MISCELLANEOUS: B.subtilis possesses two minimal, substrate-specific,
CC Tat translocases: TatAd-TatCd and TatAy-TatCy, each one composed of a
CC TatA and a TatC protein. TatA is bifunctional and performs the function
CC of both the TatA and TatB proteins of Gram-negative organisms.
CC -!- SIMILARITY: Belongs to the TatC family. {ECO:0000255|HAMAP-
CC Rule:MF_00902}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA06484.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D30808; BAA06484.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL009126; CAB12058.2; -; Genomic_DNA.
DR EMBL; X66034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; D69754; D69754.
DR RefSeq; NP_388146.2; NC_000964.3.
DR RefSeq; WP_003246495.1; NZ_JNCM01000030.1.
DR AlphaFoldDB; P42252; -.
DR SMR; P42252; -.
DR IntAct; P42252; 24.
DR STRING; 224308.BSU02640; -.
DR TCDB; 2.A.64.3.1; the twin arginine targeting (tat) family.
DR PaxDb; P42252; -.
DR EnsemblBacteria; CAB12058; CAB12058; BSU_02640.
DR GeneID; 938395; -.
DR KEGG; bsu:BSU02640; -.
DR PATRIC; fig|224308.179.peg.274; -.
DR eggNOG; COG0805; Bacteria.
DR InParanoid; P42252; -.
DR OMA; EMSFLDH; -.
DR PhylomeDB; P42252; -.
DR BioCyc; BSUB:BSU02640-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0033281; C:TAT protein transport complex; IBA:GO_Central.
DR GO; GO:0009977; F:proton motive force dependent protein transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IBA:GO_Central.
DR GO; GO:0043953; P:protein transport by the Tat complex; IBA:GO_Central.
DR HAMAP; MF_00902; TatC; 1.
DR InterPro; IPR019820; Sec-indep_translocase_CS.
DR InterPro; IPR002033; TatC.
DR PANTHER; PTHR30371; PTHR30371; 1.
DR Pfam; PF00902; TatC; 1.
DR PRINTS; PR01840; TATCFAMILY.
DR TIGRFAMs; TIGR00945; tatC; 1.
DR PROSITE; PS01218; TATC; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..242
FT /note="Sec-independent protein translocase protein TatCd"
FT /id="PRO_0000098095"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT REGION 128..149
FT /note="Interaction with TatAd"
FT REGION 171..187
FT /note="Interaction with TatAd"
FT CONFLICT 101
FT /note="L -> I (in Ref. 1; BAA06484)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="I -> IMYI (in Ref. 1; BAA06484)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 242 AA; 27706 MW; CD80471FB2D12F85 CRC64;
MDKKETHLIG HLEELRRRII VTLAAFFLFL ITAFLFVQDI YDWLIRDLDG KLAVLGPSEI
LWVYMMLSGI CAIAASIPVA AYQLWRFVAP ALTKTERKVT LMYIPGLFAL FLAGISFGYF
VLFPIVLSFL THLSSGHFET MFTADRYFRF MVNLSLPFGF LFEMPLVVMF LTRLGILNPY
RLAKARKLSY FLLIVVSILI TPPDFISDFL VMIPLLVLFE VSVTLSAFVY KKRMREETAA
AA
